SODF_CAMJJ
ID SODF_CAMJJ Reviewed; 220 AA.
AC A1VXQ2; P53640;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sodB; OrderedLocusNames=CJJ81176_0205;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8005660; DOI=10.1128/iai.62.7.2687-2694.1994;
RA Pesci E.C., Cottle D.L., Pickett C.L.;
RT "Genetic, enzymatic, and pathogenic studies of the iron superoxide
RT dismutase of Campylobacter jejuni.";
RL Infect. Immun. 62:2687-2694(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; U08132; AAA53139.1; -; Genomic_DNA.
DR EMBL; CP000538; EAQ73242.1; -; Genomic_DNA.
DR PIR; H81434; H81434.
DR RefSeq; WP_002851662.1; NC_008787.1.
DR AlphaFoldDB; A1VXQ2; -.
DR SMR; A1VXQ2; -.
DR STRING; 354242.CJJ81176_0205; -.
DR EnsemblBacteria; EAQ73242; EAQ73242; CJJ81176_0205.
DR KEGG; cjj:CJJ81176_0205; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_0_7; -.
DR OMA; KWGSFDK; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..220
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000285826"
FT BINDING 26
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 24813 MW; 1E0BE7150960D017 CRC64;
MFELRKLPYD TNAFGDFLSA ETFSYHHGKH HNTYVTNLNN LIKDTEFAGK DLVSIIKTSN
GGVFNNAAQV YNHDFYFDCI KPSTGCGCGG SCQSIDANLQ AALEKEFGSL ENFKAEFIKG
ATGVFGSGWF WLVYNTKNQK LEFVGTSNAA TPITEDKVPL LVVDVWEHAY YVDHRNARPA
YLEKFYAHIN WEFVAKAYEW ALKEGMGSVS FYANELHPVK
